TY - JOUR

T1 - Proteomic approach to characterize mitochondrial complex I from plants

AU - Klodmann, Jennifer

AU - Braun, Hans Peter

N1 - Funding information: This work was supported by the Deutsche Forschungsgemeinschaft (DFG), Grants Br1829/8-1 and Br1829/10-1.

PY - 2010/12/15

Y1 - 2010/12/15

N2 - Mitochondrial NADH dehydrogenase complex (complex I) is by far the largest protein complex of the respiratory chain. It is best characterized for bovine mitochondria and known to consist of 45 different subunits in this species. Proteomic analyses recently allowed for the first time to systematically explore complex I from plants. The enzyme is especially large and includes numerous extra subunits. Upon subunit separation by various gel electrophoresis procedures and protein identifications by mass spectrometry, overall 47 distinct types of proteins were found to form part of Arabidopsis complex I. An additional subunit, ND4L, is present but could not be detected by the procedures employed due to its extreme biochemical properties. Seven of the 48 subunits occur in pairs of isoforms, six of which were experimentally proven. Fifteen subunits of complex I from Arabidopsis are specific for plants. Some of these resemble enzymes of known functions, e.g. carbonic anhydrases and l-galactono-1,4-lactone dehydrogenase (GLDH), which catalyzes the last step of ascorbate biosynthesis. This article aims to review proteomic data on the protein composition of complex I in plants. Furthermore, a proteomic re-evaluation on its protein constituents is presented.

AB - Mitochondrial NADH dehydrogenase complex (complex I) is by far the largest protein complex of the respiratory chain. It is best characterized for bovine mitochondria and known to consist of 45 different subunits in this species. Proteomic analyses recently allowed for the first time to systematically explore complex I from plants. The enzyme is especially large and includes numerous extra subunits. Upon subunit separation by various gel electrophoresis procedures and protein identifications by mass spectrometry, overall 47 distinct types of proteins were found to form part of Arabidopsis complex I. An additional subunit, ND4L, is present but could not be detected by the procedures employed due to its extreme biochemical properties. Seven of the 48 subunits occur in pairs of isoforms, six of which were experimentally proven. Fifteen subunits of complex I from Arabidopsis are specific for plants. Some of these resemble enzymes of known functions, e.g. carbonic anhydrases and l-galactono-1,4-lactone dehydrogenase (GLDH), which catalyzes the last step of ascorbate biosynthesis. This article aims to review proteomic data on the protein composition of complex I in plants. Furthermore, a proteomic re-evaluation on its protein constituents is presented.

KW - Arabidopsis thaliana

KW - Carbonic anhydrase

KW - Complex I

KW - Mitochondria

KW - NADH dehydrogenase

KW - Respiratory chain

UR - http://www.scopus.com/inward/record.url?scp=79958144995&partnerID=8YFLogxK

U2 - 10.1016/j.phytochem.2010.11.012

DO - 10.1016/j.phytochem.2010.11.012

M3 - Article

C2 - 21167537

AN - SCOPUS:79958144995

VL - 72

SP - 1071

EP - 1080

JO - PHYTOCHEMISTRY

JF - PHYTOCHEMISTRY

SN - 0031-9422

IS - 10

ER -